Details for: MTREX

Gene ID: 23517

Symbol: MTREX

Ensembl ID: ENSG00000039123

Description: Mtr4 exosome RNA helicase

Associated with

Other Information

Genular Protein ID: 1160870178

Symbol: MTREX_HUMAN

Name: ATP-dependent RNA helicase SKIV2L2

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 7584044

Title: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1.

PubMed ID: 7584044

DOI: 10.1093/dnares/1.5.223

PubMed ID: 16782053

Title: The AAA-ATPase NVL2 is a component of pre-ribosomal particles that interacts with the DExD/H-box RNA helicase DOB1.

PubMed ID: 16782053

DOI: 10.1016/j.bbrc.2006.06.017

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11719186

Title: AU binding proteins recruit the exosome to degrade ARE-containing mRNAs.

PubMed ID: 11719186

DOI: 10.1016/s0092-8674(01)00578-5

PubMed ID: 12429849

Title: Functional proteomic analysis of human nucleolus.

PubMed ID: 12429849

DOI: 10.1091/mbc.e02-05-0271

PubMed ID: 11991638

Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.

PubMed ID: 11991638

DOI: 10.1017/s1355838202021088

PubMed ID: 16263084

Title: Zcchc8 is a glycogen synthase kinase-3 substrate that interacts with RNA-binding proteins.

PubMed ID: 16263084

DOI: 10.1016/j.bbrc.2005.10.090

PubMed ID: 17412707

Title: C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are involved in pre-rRNA processing.

PubMed ID: 17412707

DOI: 10.1093/nar/gkm082

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21855801

Title: Interaction profiling identifies the human nuclear exosome targeting complex.

PubMed ID: 21855801

DOI: 10.1016/j.molcel.2011.06.028

PubMed ID: 22817747

Title: Comparison of the yeast and human nuclear exosome complexes.

PubMed ID: 22817747

DOI: 10.1042/bst20120061

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 26166824

Title: NVL2, a nucleolar AAA-ATPase, is associated with the nuclear exosome and is involved in pre-rRNA processing.

PubMed ID: 26166824

DOI: 10.1016/j.bbrc.2015.07.032

PubMed ID: 26456651

Title: AAA-ATPase NVL2 acts on MTR4-exosome complex to dissociate the nucleolar protein WDR74.

PubMed ID: 26456651

DOI: 10.1016/j.bbrc.2015.09.160

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 27871484

Title: Identification of a nuclear exosome decay pathway for processed transcripts.

PubMed ID: 27871484

DOI: 10.1016/j.molcel.2016.09.025

PubMed ID: 27905398

Title: Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors.

PubMed ID: 27905398

DOI: 10.1038/ncomms13573

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 29107693

Title: WDR74 participates in an early cleavage of the pre-rRNA processing pathway in cooperation with the nucleolar AAA-ATPase NVL2.

PubMed ID: 29107693

DOI: 10.1016/j.bbrc.2017.10.148

PubMed ID: 29902117

Title: NRDE-2, the human homolog of fission yeast Nrl1, prevents DNA damage accumulation in human cells.

PubMed ID: 29902117

DOI: 10.1080/15476286.2018.1467180

PubMed ID: 30538148

Title: Human nuclear RNAi-defective 2 (NRDE2) is an essential RNA splicing factor.

PubMed ID: 30538148

DOI: 10.1261/rna.069773.118

PubMed ID: 29906447

Title: Helicase-Dependent RNA Decay Illuminated by a Cryo-EM Structure of a Human Nuclear RNA Exosome-MTR4 Complex.

PubMed ID: 29906447

DOI: 10.1016/j.cell.2018.05.041

PubMed ID: 29844170

Title: Structural basis for MTR4-ZCCHC8 interactions that stimulate the MTR4 helicase in the nuclear exosome-targeting complex.

PubMed ID: 29844170

DOI: 10.1073/pnas.1803530115

PubMed ID: 30842217

Title: NRDE2 negatively regulates exosome functions by inhibiting MTR4 recruitment and exosome interaction.

PubMed ID: 30842217

DOI: 10.1101/gad.322602.118

PubMed ID: 31358741

Title: The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs.

PubMed ID: 31358741

DOI: 10.1038/s41467-019-11339-x

Sequence Information:

  • Length: 1042
  • Mass: 117805
  • Checksum: 49F47BEC753FBEE7
  • Sequence:
  • MADAFGDELF SVFEGDSTTA AGTKKDKEKD KGKWKGPPGS ADKAGKRFDG KLQSESTNNG 
    KNKRDVDFEG TDEPIFGKKP RIEESITEDL SLADLMPRVK VQSVETVEGC THEVALPAEE 
    DYLPLKPRVG KAAKEYPFIL DAFQREAIQC VDNNQSVLVS AHTSAGKTVC AEYAIALALR 
    EKQRVIFTSP IKALSNQKYR EMYEEFQDVG LMTGDVTINP TASCLVMTTE ILRSMLYRGS 
    EVMREVAWVI FDEIHYMRDS ERGVVWEETI ILLPDNVHYV FLSATIPNAR QFAEWICHLH 
    KQPCHVIYTD YRPTPLQHYI FPAGGDGLHL VVDENGDFRE DNFNTAMQVL RDAGDLAKGD 
    QKGRKGGTKG PSNVFKIVKM IMERNFQPVI IFSFSKKDCE AYALQMTKLD FNTDEEKKMV 
    EEVFSNAIDC LSDEDKKLPQ VEHVLPLLKR GIGIHHGGLL PILKETIEIL FSEGLIKALF 
    ATETFAMGIN MPARTVLFTN ARKFDGKDFR WISSGEYIQM SGRAGRRGMD DRGIVILMVD 
    EKMSPTIGKQ LLKGSADPLN SAFHLTYNMV LNLLRVEEIN PEYMLEKSFY QFQHYRAIPG 
    VVEKVKNSEE QYNKIVIPNE ESVVIYYKIR QQLAKLGKEI EEYIHKPKYC LPFLQPGRLV 
    KVKNEGDDFG WGVVVNFSKK SNVKPNSGEL DPLYVVEVLL RCSKESLKNS ATEAAKPAKP 
    DEKGEMQVVP VLVHLLSAIS SVRLYIPKDL RPVDNRQSVL KSIQEVQKRF PDGIPLLDPI 
    DDMGIQDQGL KKVIQKVEAF EHRMYSHPLH NDPNLETVYT LCEKKAQIAI DIKSAKRELK 
    KARTVLQMDE LKCRKRVLRR LGFATSSDVI EMKGRVACEI SSADELLLTE MMFNGLFNDL 
    SAEQATALLS CFVFQENSSE MPKLTEQLAG PLRQMQECAK RIAKVSAEAK LEIDEETYLS 
    SFKPHLMDVV YTWATGATFA HICKMTDVFE GSIIRCMRRL EELLRQMCQA AKAIGNTELE 
    NKFAEGITKI KRDIVFAASL YL

Genular Protein ID: 2387307956

Symbol: Q3MHC9_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

Sequence Information:

  • Length: 67
  • Mass: 7336
  • Checksum: 9A4E0689BFCACC89
  • Sequence:
  • MADAFGDELF SVFEGDSTTA AGTKKDKEKD KGKWKGPPGS ADKAGKRFDG KLQSESTKKK 
    KKKKKKK

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.